CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003636
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H2A.Z 
Protein Synonyms/Alias
 H2A/z 
Gene Name
 H2AFZ 
Gene Synonyms/Alias
 H2AZ 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MAGGKAGKDSGKacetylation[1, 2, 3, 4, 5, 6, 7, 8]
8MAGGKAGKDSGKAKTacetylation[4, 5, 6, 7, 8]
12KAGKDSGKAKTKAVSacetylation[5, 6, 7, 8]
14GKDSGKAKTKAVSRSacetylation[6, 8]
102EELDSLIKATIAGGGubiquitination[9, 10, 11]
116GVIPHIHKSLIGKKGacetylation[8, 12]
116GVIPHIHKSLIGKKGubiquitination[9, 10, 11, 12, 13, 14, 15, 16]
121IHKSLIGKKGQQKTVubiquitination[9, 10, 11, 12, 13, 14, 15, 16, 17]
122HKSLIGKKGQQKTV*ubiquitination[9, 10, 11, 12, 13, 14, 15, 16, 17]
126IGKKGQQKTV*****ubiquitination[9, 11, 16, 17]
Reference
 [1] Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase.
 Verreault A, Kaufman PD, Kobayashi R, Stillman B.
 Curr Biol. 1998 Jan 15;8(2):96-108. [PMID: 9427644]
 [2] Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates.
 Schiltz RL, Mizzen CA, Vassilev A, Cook RG, Allis CD, Nakatani Y.
 J Biol Chem. 1999 Jan 15;274(3):1189-92. [PMID: 9880483]
 [3] Tip60 acetylates six lysines of a specific class in core histones in vitro.
 Kimura A, Horikoshi M.
 Genes Cells. 1998 Dec;3(12):789-800. [PMID: 10096020]
 [4] Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry.
 Bonenfant D, Coulot M, Towbin H, Schindler P, van Oostrum J.
 Mol Cell Proteomics. 2006 Mar;5(3):541-52. [PMID: 16319397]
 [5] Quantitative proteomic analysis of post-translational modifications of human histones.
 Beck HC, Nielsen EC, Matthiesen R, Jensen LH, Sehested M, Finn P, Grauslund M, Hansen AM, Jensen ON.
 Mol Cell Proteomics. 2006 Jul;5(7):1314-25. [PMID: 16627869]
 [6] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [7] Acetylation of vertebrate H2A.Z and its effect on the structure of the nucleosome.
 Ishibashi T, Dryhurst D, Rose KL, Shabanowitz J, Hunt DF, Ausió J.
 Biochemistry. 2009 Jun 9;48(22):5007-17. [PMID: 19385636]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [11] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [12] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [13] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [14] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [15] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [16] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [17] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
 Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. 
Sequence Annotation
 REGION 2 17 Required for interaction with INCENP (By
 REGION 93 103 Required for interaction with INCENP (By
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 5 5 N6-acetyllysine.
 MOD_RES 8 8 N6-acetyllysine.
 MOD_RES 12 12 N6-acetyllysine.
 MOD_RES 14 14 N6-acetyllysine.
 CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Chromosome; Complete proteome; DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 128 AA 
Protein Sequence
MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE 60
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG 120
KKGQQKTV 128 
Gene Ontology
 GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0006334; P:nucleosome assembly; IEA:InterPro. 
Interpro
 IPR009072; Histone-fold.
 IPR007125; Histone_core_D.
 IPR002119; Histone_H2A. 
Pfam
 PF00125; Histone 
SMART
 SM00414; H2A 
PROSITE
 PS00046; HISTONE_H2A 
PRINTS
 PR00620; HISTONEH2A.